(C) 2011 Elsevier Ltd. All rights reserved.”
“Although protein Z ( PZ) has a domain arrangement similar to the essential coagulation proteins FVII, FIX, FX, and protein C, its serine

protease ( SP)- like domain is incomplete and does not exhibit proteolytic activity. We have generated a trial sequence of putative activated protein Z ( PZa) by identifying amino acid mutations in the SP- like domain that might reasonably resurrect the serine protease catalytic activity of PZ. The structure of the activated form was then modeled based on the proposed sequence using homology modeling and solvent- equilibrated molecular dynamics simulations. In silico docking of inhibitors of FVIIa and FXa to the putative active site of equilibrated PZa, along with structural comparison with its homologous proteins, PLX3397 molecular weight suggest that the designed PZa can possibly act as a serine protease.”
“The left-handed beta-helix (L beta H) has received interest recently

as it folds as a possible solution for the structure of misfolded proteins associated with prion and Huntington’s diseases. Through a combination of sequence and structure analysis, we uncover a novel feature that is common to this unique fold: a two-fold symmetry in both sequence and structure, and this feature always coupled with extended loops in the middle of the www.selleckchem.com/products/AC-220.html helix. Since the results reveal a two-fold symmetric pattern both in the sequence and structure, it may indicate that the symmetry in tertiary structure is coded by the symmetry in primary sequence, which agrees with Anfisen’s proposal that a protein’s amino-acid sequence specify its three-dimensional structure. It 4��8C may also indicate that L beta H adopts

a two-fold repeat pattern during the evolution process and symmetry helps maintaining the stability of the helix structure. The two-fold symmetric pattern and extended loops might be important in maintaining stability of helix proteins. This discovery can be useful in understanding the folding mechanisms of this protein fold and provide insights in the relation between sequences and structures. (C) 2011 Elsevier Ltd. All rights reserved.”
“Dioxygenases catalyze dioxygen incorporation into various organic compounds and play a key role in the complex degradation pathway of mono- and polycyclic aromatic and hetero- aromatic compounds. Here we report the crystal structure of gentisate 1,2- dioxygenase from Silicibacter pomeroyi ( GDOsp) at a 2.8 A resolution. The enzyme possessed a conserved three- dimensional structure of the bicupin family, forming a homotetramerization. However, each subunit of GDOsp unusually contained two ferrous centers that were located in its two homologous cupin domains, respectively. Further mutagenic analysis indicated that the enzyme activity of GDOsp depends on the microenvironment in both metal- binding sites.